Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174

Molecular Cell
Marc C MoraisMichael G Rossmann

Abstract

The three-dimensional structure of bacteriophage phiX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 angstroms by X-ray crystallography. The crystals belong to space group P4(1)2(1)2 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the phiX174 procapsid structure. Furthermore, application of the crystallographic 4(1) symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.

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Citations

Aug 11, 2012·The Journal of Biological Chemistry·G Pauline Padilla-MeierSherwood R Casjens
Oct 14, 2011·Viruses·Anastasia A Aksyuk, Michael G Rossmann
May 10, 2005·Proceedings of the National Academy of Sciences of the United States of America·Andrei FokineMichael G Rossmann
Jul 8, 2016·Journal of Molecular Evolution·Geoffrey S Diemer, Kenneth M Stedman
May 18, 1999·Journal of Molecular Biology·T DoklandM G Rossmann
Feb 14, 2016·Virology·Sarah M Doore, Bentley A Fane

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